The sliding filament theory explains how muscles contract at the molecular level through the interaction of two key proteins: myosin and actin. Here's an overview of myosin and actin in the context of the sliding filament theory:
1. Actin:
Actin is a globular protein that forms thin filaments in muscle fibers.
Actin filaments are arranged in a double helix structure and are anchored to the Z-discs at the ends of the sarcomere.
Actin has binding sites that interact with myosin during muscle contraction.
When calcium ions bind to regulatory proteins on actin (troponin and tropomyosin), they expose these binding sites, allowing myosin to attach.
2. Myosin:
Myosin is a motor protein that forms thick filaments in muscle fibers.
Myosin molecules have a tail region and a globular head region.
The myosin heads contain ATP-binding sites and actin-binding sites.
During muscle contraction, myosin heads bind to actin filaments and undergo a conformational change, pulling the actin filaments towards the center of the sarcomere.
3. Cross-Bridge Formation:
The interaction between myosin and actin is known as the cross-bridge cycle.
When calcium ions bind to actin, myosin heads bind to actin at the actin-binding sites, forming cross-bridges.
ATP is hydrolyzed to provide energy for the myosin heads to pivot and generate force, pulling the actin filaments towards the center of the sarcomere.
4. Muscle Contraction:
As myosin heads pull on actin filaments, the sarcomeres shorten, and the muscle fiber contracts.
The repeated formation and release of cross-bridges allow for the sliding of actin filaments along myosin filaments, resulting in muscle contraction.
This process occurs in a coordinated manner throughout the muscle fiber, leading to overall muscle contraction.